Structure of PDB 4f79 Chain A

Receptor sequence
>4f79A (length=478) Species: 1309 (Streptococcus mutans) [Search protein sequence]
AMSKLPENFLWGGAVAAHQLEGGWQEGGKGISVADVMTAGRHGVAREITA
GVLEGKYYPNHEAIDFYHHYKEDVKLFAEMGFKCFRTSIAWTRIFPKGDE
AEPNEAGLQFYDDLFDECLKYGIEPVVTLSHFELPYHLVTEYGGFTNRKV
IDFFVHFAEVCFRRYKDKVKYWMTFNEINNQANYQEDFAPFTNSGIVYKE
GDDREAIMYQAAHYELVASARAVKIGHAINPNLNIGCMVAMCPIYPATCN
PKDILMAQKAMQKRYYFADVHVHGFYPEHIFKYWERKAIKVDFTERDKKD
LFEGTVDYIGFSYYMSFVIDAHRENNPYYDYLETEDLVKNPYVKASDWDW
QIDPQGLRYALNWFTDMYHLPLFIVQNGFGAIDQVEADGMVHDDYRIDYL
GAHIKEMIKAVDEDGVELMGYTPWGCIDLVSAGTGEMRKRYGFIYVDKDD
EGKGTLKRSPKLSFNWYKEVIASNGDDI
3D structure
PDB4f79 GH1-family 6-P-beta-glucosidases from human microbiome lactic acid bacteria.
ChainA
Resolution2.54 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R85 H130 E176 N179 S311 Y313 Q375
Catalytic site (residue number reindexed from 1) R86 H131 E177 N180 S312 Y314 Q376
Enzyme Commision number 3.2.1.86: 6-phospho-beta-glucosidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 P53 A Q18 H130 F131 E176 Y313 W349 Q375 W423 S430 A431 G432 K438 Y440 Q19 H131 F132 E177 Y314 W350 Q376 W424 S431 A432 G433 K439 Y441
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008422 beta-glucosidase activity
GO:0008706 6-phospho-beta-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0016052 carbohydrate catabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4f79, PDBe:4f79, PDBj:4f79
PDBsum4f79
PubMed23519420
UniProtQ8DT00

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